Molecular characterization of a novel intracellular ADP-ribosyl cyclase

Dev Churamani, Michael J. Boulware, Timothy J. Geach, Andrew C R Martin, Gary W. Moy, Yi Hslen Su, Victor D. Vacquier, Jonathan S. Marchant, Leslie Dale, Sandip Patel

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


Background. ADP-ribosyl cyclases are remarkable enzymes capable of catalyzing multiple reactions including the synthesis of the novel and potent intracellular calcium mobilizing messengers, cyclic ADP-ribose and NAADP. Not all ADP-ribosyl cyclases however have been characterized at the molecular level. Moreover, those that have are located predominately at the outer cell surface and thus away from their cytosolic substrates. Methodology/Principal Findings. Here we report the molecular cloning of a novel expanded family of ADP-ribosyl cyclases from the sea urchin, an extensively used model organism for the study of inositol trisphosphate-independent calcium mobilization. We provide evidence that one of the isoforms (SpARC1) is a soluble protein that is targeted exclusively to the endoplasmic reticulum lumen when heterologously expressed. Catalytic activity of the recombinant protein was readily demonstrable in crude cell homogenates, even under conditions where luminal continuity was maintained. Conclusions/Significance. Our data reveal a new intracellular location for ADP-ribosyl cyclases and suggest that production of calcium mobilizing messengers may be compartmentalized.

Original languageEnglish (US)
Article numbere797
JournalPloS one
Issue number8
StatePublished - Aug 29 2007


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